کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2016909 | 1542039 | 2016 | 28 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Constitutive over-expression of rice ClpD1 protein enhances tolerance to salt and desiccation stresses in transgenic Arabidopsis plants
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کلمات کلیدی
Oryza sativaneomycin phosphotransferase IIisopropylthio-β-galactosidepyrroline-5-carboxylate synthasesqRT-PCRnptIIPB1NBDChaperoneP5CSCLPGSTProDHIPTGDASORFArabidopsis thaliana - آرابیدوپسیس تالیاناAlpha amylase - آلفا آمیلازOsmotic stress - استرس اسمزیAMY - امیSalt stress - تنش شوریnucleotide binding domain - دامنه اتصال نوکلئوتیدیDAG - روزdays after germination - روز بعد از جوانه زدنCitrate synthase - سیترات سیتواستاتopen reading frame - قاب خواندن بازReaction - واکنشCaseinolytic protease - پروتئاز کازئینولیتیکproline dehydrogenase - پرولین دهیدروژنازPoly ethylene glycol - پلی اتیلن گلیکولPEG - پلیاتیلن گلیکول glutathione S-transferase - گلوتاتیون S-ترانسفراز
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Constitutive over-expression of rice ClpD1 protein enhances tolerance to salt and desiccation stresses in transgenic Arabidopsis plants Constitutive over-expression of rice ClpD1 protein enhances tolerance to salt and desiccation stresses in transgenic Arabidopsis plants](/preview/png/2016909.png)
چکیده انگلیسی
Caseinolytic proteases (Clps) perform the important role of removing protein aggregates from cells, which can otherwise prove to be highly toxic. ClpD system is a two-component protease complex composed of a regulatory ATPase module ClpD and a proteolytic component ClpP. Under desiccation stress condition, rice ClpD1 (OsClpD1) gene encoding for the regulatory subunit, was represented by four variant transcripts differing mainly in the expanse of their N-terminal amino acids. These transcripts were expressed in a differential manner in response to salt, mannitol and polyethylene glycol stresses in rice. Purified OsClpD1.3 protein exhibited intrinsic chaperone activity, shown using citrate synthase as substrate. Arabidopsis (Col-0) plants over-expressing OsClpD1.3 open reading frame downstream to CaMV35S promoter (ClpD1.3 plants) showed higher tolerance to salt and desiccation stresses as compared to wild type plants. ClpD1.3 seedlings also showed enhanced growth during the early stages of seed germination under unstressed, control conditions. The free proline levels and starch breakdown activities were higher in the ClpD1.3 seedlings as compared to the wild type Arabidopsis seedlings. It thus emerges that increasing the potential of ClpD1 chaperoning activity may be of advantage in protection against abiotic stresses.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Plant Science - Volume 250, September 2016, Pages 69-78
Journal: Plant Science - Volume 250, September 2016, Pages 69-78
نویسندگان
Ratnesh Chandra Mishra, Richa Richa, Anil Grover,